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0SNP25_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSNAP25
DescriptionSynaptosomal-associated protein 25 (snap-25) (synaptosomal-associated 25 kda protein) (super protein) (sup).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005515 protein binding (IPI)
0007269 neurotransmitter secretion (NAS)
0001504 neurotransmitter uptake (NAS)
0050796 regulation of insulin secretion (TAS)
0007268 synaptic transmission (NAS)
0016081 synaptic vesicle docking during exocytosis (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains assigned to SynO:
SNAP-25 (synaptosome-associated protein 25 kDa) proteins are components of SNARE complexes.hich are proposed to account for the specificity of membrane fusion and to directly execute fusion by forming a tight complex (the SNARE or core complex) that brings the synaptic vesicle and plasma membranes together. The SNAREs constitute a large family of proteins that are characterized by 60-residue sequences known as SNARE motifs ().hich have a high propensity to form coiled coils and often precede carboxy-terminal transmembrane regions. The synaptic core complex is formed by four SNARE motifs (two from SNAP25 and one each from synaptobrevin and syntaxin 1) that are unstructured in isolation but form a parallel four-helix bundle on assembly. The crystal structure of the core complex revealed that the helix bundle is highly twisted and contains several salt bridges on the surface.s well as layers of interior hydrophobic residues. However. polar layer in the centre of the complex is formed by three glutamines (two from SNAP25 and one from syntaxin 1) and one arginine (from synaptobrevin) . Members of the SNAP-25 family contain a cluster of cysteine residues that can be palmitoylated for membrane attachment .
  IPR000928:SNAP-25
The process of vesicular fusion with target membranes depends on a set of SNAREs (SNAP-Receptors).hich are associated with the fusing membranes . Target SNAREs (t-SNAREs) are localised on the target membrane and belong to two different families.he syntaxin-like family and the SNAP-25 like family. One member of each family.ogether with av-SNARE localised on the vesicular membrane.re required for fusion. The Syntaxins are type-I transmembrane proteins that contain several regions with coiled-coil propensity in their cytosolic part.he SNARE motif. SNAP-25 () is a protein consisting of two coiled-coil regions.hich is associated with the membrane by lipid anchors. SNARE motifs assemble into parallel four helix bundles stabilised by the burial of these hydrophobic helix faces in the bundle core. Monomeric SNARE motifs are disordered so this assembly reaction is accompanied by a dramatic increase in alpha-helical secondary structure . The parallel arrangement of SNARE motifs within complexes bring the transmembrane anchors.nd the two membranes.nto close proximity. Recently.t was shown that the two coiled-coil regions of SNAP-25 andone of the coiled-coil regions of the syntaxins are related . This domain is found in both Syntaxin and SNAP-25 families as well as in other proteins.
  IPR000727:Target SNARE coiled-coil region
Soluble N-ethylmaleimide attachment protein receptor (SNARE) proteins are a family of membrane-associated proteins characterised by an alpha-helical coiled-coil domain called the SNARE motif . These proteins are classified as v-SNAREs and t-SNAREs based on their localisation on vesicle or target membrane; another classification scheme defines R-SNAREs and Q-SNAREs.s based on the conserved arginine or glutamine residue in the centre of the SNARE motif. SNAREs are localised to distinct membrane compartments of the secretory and endocytic trafficking pathways.nd contribute to the specificity of intracellular membrane fusion processes.The t-SNARE domain consists of a 4-helical bundle with a coiled-coil twist. The SNARE motif contributes to the fusion of two membranes. SNARE motifs fall into four classes: homologues of syntaxin 1a (t-SNARE).AMP-2 (v-SNARE).nd the N- and C-terminal SNARE motifs of SNAP-25. It is thought that one member from each class interacts to form a SNARE complex.The SNARE motif represented in this entry is found in the N-terminal domains of certain syntaxin family members: syntaxin 1a.hich is required for neurotransmitter release.yntaxin 6.hich is found in endosomal transport vesicles .east Sso1p .nd Vam3p. yeast syntaxin essential for vacuolar fusion . The SNARE motifs in these proteins share structural similarity.espite having a low level of sequence similarity.
  IPR010989:t-snare
IPR000928:SNAP-25 
Evalue:-23.1366767883301 
Location:91-141IPR000727:SNARE 
Evalue:-17.6575775146484 
Location:145-204IPR000727:t_SNARE 
Evalue:-11.7212463990472 
Location:14-81
SequencesProtein: SNP25_HUMAN (206 aa)
mRNA: NM_130811
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords,domains)
Fusion of intracellular membrane-bound vesicles with the pre-synaptic membrane of the neuronal cell resulting in release of neurotransmitter into the synaptic cleft.
sdb:0049 synaptic vesicle fusion  (Evidence:keywords,domains)
Typical ecretory organelles, some 50 nm in diameter, of presynaptic nerve terminals; accumulate high concentrations of nonpeptide neurotransmitters and secrete these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
sdb:0094 typical synaptic vesicle  (Evidence:keywords,domains)
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords,domains)
priming for exocytosis prepares the calcium-dependent release and may involve partial fusion process. The vesicles are primed and become responsive to calcium.
sdb:0120 priming  (Evidence:keywords,domains)
?
sdb:0145 regulation of uptake of transmitters  (Evidence:keywords,domains)
attachment of the vesicle filled with transmitters involves a specific interaction between the vesicle membrane and the presynaptic active zone.
sdb:0148 docking  (Evidence:keywords,domains)
?
sdb:0223 transmitter release  (Evidence:keywords,domains)
?
sdb:0328 transmitters release and endocytosis  (Evidence:keywords,domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 50 residues, 10147476-10147625Exon2: 47 residues, 10204076-10204211Exon3: 16 residues, 10206332-10206374Exon4: 18 residues, 10213371-10213420Exon5: 41 residues, 10221808-10221926Exon6: 44 residues, 10225572-10225698Exon7: 50 residues, 10227915-10228060Exon8: 431 residues, 10234776-10236065Exon9: 2 residues, -Jump to SNP25_HUMAN  
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